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Molecular cloning of a new human G protein Evidence for two G iα ‐like protein families
Author(s) -
Didsbury John R.,
Snyderman Ralph
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81228-0
Subject(s) - cloning (programming) , molecular cloning , computational biology , genetics , biology , chemistry , peptide sequence , gene , computer science , programming language
The amino acid sequence of a novel G protein α subunit (G xα ) has been deduced from the nucleotide sequence of a human cDNA clone isolated from a differentiated HL‐60 cDNA library. The cDNA encodes a polypeptide of 354 amino acids ( M r 40 519) which is closely related to G iα proteins. The amino acid sequence homology between G xα and human myeloid G iα is 86% with 15 nonconservative substitutions. G xα also shares 86% homology with both rat brain and mouse macrophage G iα but is more homologous (94%) to bovine brain G iα with only 5 nonconservative amino acid differences. G proteins previously termed G iα may fall into at least two distinct groups, with one including human myeloid G iα , rat brain G iα and mouse macrophage G iα ; and other G xα ; and bovine brain G iα . One group probably contains true G i and the other a new class of G protein whose function remains to be determined.